ID   TRPB2_VIBPA             Reviewed;         407 AA.
AC   Q87IM1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Tryptophan synthase beta chain 2;
DE            EC=4.2.1.20;
GN   Name=trpB2; OrderedLocusNames=VPA0585;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC         Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR   EMBL; BA000032; BAC61928.1; -; Genomic_DNA.
DR   RefSeq; NP_800095.1; NC_004605.1.
DR   RefSeq; WP_005482634.1; NC_004605.1.
DR   AlphaFoldDB; Q87IM1; -.
DR   SMR; Q87IM1; -.
DR   STRING; 223926.28808751; -.
DR   EnsemblBacteria; BAC61928; BAC61928; BAC61928.
DR   KEGG; vpa:VPA0585; -.
DR   PATRIC; fig|223926.6.peg.3526; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_6; -.
DR   OMA; QWGMAVS; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002493; Chromosome 2.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00263; trpB; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..407
FT                   /note="Tryptophan synthase beta chain 2"
FT                   /id="PRO_0000099020"
FT   MOD_RES         94
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  44250 MW;  014840BC7FC1822A CRC64;
     MKNSFDHNMP NNEGYFGEYG GSFVPPELEQ IMRDINAAYE ECCQDPEFKD ELARLYKHFV
     GRPSPIFHAA NLSKKYGADI YLKREDLNHT GAHKINHCLG EAILAKKMGK KKLIAETGAG
     QHGVALATAA ALVGLECDIY MGEVDIAKEH PNVVRMRILG ANVIPATHGR KTLKEAVDAA
     FEAYLKDPET QLYAIGSVVG PHPFPKMVRD FQSIIGNEAR VQFKEMTGKL PNNLVACVGG
     GSNAMGLFSA FLEDENVAIH GVEPAGRSLD KVGEHAATLT LGEPGIMHGF KSYMLKDEQG
     EPQEVHSVAS GLDYPSVGPQ HSYLKDIGRV NYGSINDDEA IDAFFELSRE EGIIPAIESS
     HAVAYAIKLA QQGESGSILV NLSGRGDKDI DFVVENYGAK YGIESLI